This thesis was aimed at the over-expression of the extracellular N-terminal domain (ECD) of the human a7 nicotinic acetylcholine receptor (nAChR). The ECD of the a7 nAChR is more suitable than the ECD of other nAChR subunits for crystallographic studies, mainly because the receptor is oligomeric and does not require any other nAChR subunit ECD to form a complete agonist/antagonist binding domain.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:493414 |
| Date | January 2005 |
| Creators | Ferrandon, Sebastien |
| Publisher | Oxford Brookes University |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
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